Hormonal modulation of structural alteration of rat ovarian luteinizing/human chorionic gonadotropin receptors.

The structure-stabilizing effect of homologous and heterogeneous desensitization and albumin on rat ovarian LH/hCG receptors was analyzed by thermal perturbation technique. HCG-induced down-regulation shifted the heat inactivation profile of hCG-binding sites to a temperature lower by about 7 degrees C (T50 values). In heterogeneous desensitization, which also involves uncoupling of receptors from adenylyl cyclase system, only follicle stimulating hormone (FSH) changed the stability of ovarian LH/hCG receptors. Stimulation of other hormonal receptors, which belong to the family of membrane spanning G protein-linked receptors, i.e. beta-adrenergic, glucagon, serotonin and prostaglandin E (PGE) had no effect on the stability of the LH/hCG receptor. Reduction of the stability of the LH/hCG receptor by about 3 degrees C after PGF2alpha injection to luteinized rats may be connected with specific process of luteolysis. On the other hand, albumin had a stabilizing effect on the receptor. The receptor destabilizing action of oleic acid incorporated into ovarian membranes along with calcium stimulation of endogenous phospholipase A (PLA) activity and reversal of these effects when BSA was used as fatty acid scavenger, may indicate that free fatty acids are responsible for the thermal instability of hCG-binding sites. Fluorescence quenching studies indicated that extraction of free fatty acids by albumin elevated the accessibility of fluorophores for acrylamide, and suggest that modificated lipid-protein interactions may affect the stability of the LH/hCG receptor structure.